data_30200 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 30200 _Entry.Title ; Sparse-restraint solution NMR structure of micelle-solubilized cytosolic amino terminal domain of C. elegans mechanosensory ion channel MEC-4 refined by restrained Rosetta ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2016-11-04 _Entry.Accession_date 2016-11-04 _Entry.Last_release_date 2017-01-24 _Entry.Original_release_date 2017-01-24 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 J. Everett J. K. . . 30200 2 G. Liu G. . . . 30200 3 B. Mao B. . . . 30200 4 M. Driscoll M. A. . . 30200 5 G. Montelione G. T. . . 30200 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 PSI:Biology 'Northeast Structural Genomics Consortium' NESG 30200 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID NESG . 30200 'Northeast Structural Genomics Consortium' . 30200 PSI-Biology . 30200 'Structural Genomics' . 30200 'TRANSPORT PROTEIN' . 30200 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 30200 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 287 30200 '15N chemical shifts' 91 30200 '1H chemical shifts' 91 30200 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2017-01-26 . original BMRB . 30200 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 5TTT 'BMRB Entry Tracking System' 30200 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 30200 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Sparse-restraint solution NMR structure of micelle-solubilized cytosolic amino terminal domain of C. elegans mechanosensory ion channel MEC-4 refined by restrained Rosetta ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD 0353 _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 J. Everett J. K. . . 30200 1 2 G. Liu G. . . . 30200 1 3 B. Mao B. . . . 30200 1 4 M. Driscoll M. A. . . 30200 1 5 G. Montelione G. T. . . 30200 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 30200 _Assembly.ID 1 _Assembly.Name 'Degenerin mec-4' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 entity_1 1 $entity_1 A A yes . . . . . . 30200 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 30200 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MSWMQNLKNYQHLRDPSEYM SQVYGDPLAYLQETTKFVTE REYYEDFGYGECFNSTESEV QCELITGEFDPKLLPYDKRL AWHFKEFCYKTSAHGIPMIG EAPLEHHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer no _Entity.Nstd_chirality . _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 111 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID 1 _Entity.Fragment 'residues 1-103' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 13296.793 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Mechanosensory abnormality protein 4' na 30200 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 30200 1 2 . SER . 30200 1 3 . TRP . 30200 1 4 . MET . 30200 1 5 . GLN . 30200 1 6 . ASN . 30200 1 7 . LEU . 30200 1 8 . LYS . 30200 1 9 . ASN . 30200 1 10 . TYR . 30200 1 11 . GLN . 30200 1 12 . HIS . 30200 1 13 . LEU . 30200 1 14 . ARG . 30200 1 15 . ASP . 30200 1 16 . PRO . 30200 1 17 . SER . 30200 1 18 . GLU . 30200 1 19 . TYR . 30200 1 20 . MET . 30200 1 21 . SER . 30200 1 22 . GLN . 30200 1 23 . VAL . 30200 1 24 . TYR . 30200 1 25 . GLY . 30200 1 26 . ASP . 30200 1 27 . PRO . 30200 1 28 . LEU . 30200 1 29 . ALA . 30200 1 30 . TYR . 30200 1 31 . LEU . 30200 1 32 . GLN . 30200 1 33 . GLU . 30200 1 34 . THR . 30200 1 35 . THR . 30200 1 36 . LYS . 30200 1 37 . PHE . 30200 1 38 . VAL . 30200 1 39 . THR . 30200 1 40 . GLU . 30200 1 41 . ARG . 30200 1 42 . GLU . 30200 1 43 . TYR . 30200 1 44 . TYR . 30200 1 45 . GLU . 30200 1 46 . ASP . 30200 1 47 . PHE . 30200 1 48 . GLY . 30200 1 49 . TYR . 30200 1 50 . GLY . 30200 1 51 . GLU . 30200 1 52 . CYS . 30200 1 53 . PHE . 30200 1 54 . ASN . 30200 1 55 . SER . 30200 1 56 . THR . 30200 1 57 . GLU . 30200 1 58 . SER . 30200 1 59 . GLU . 30200 1 60 . VAL . 30200 1 61 . GLN . 30200 1 62 . CYS . 30200 1 63 . GLU . 30200 1 64 . LEU . 30200 1 65 . ILE . 30200 1 66 . THR . 30200 1 67 . GLY . 30200 1 68 . GLU . 30200 1 69 . PHE . 30200 1 70 . ASP . 30200 1 71 . PRO . 30200 1 72 . LYS . 30200 1 73 . LEU . 30200 1 74 . LEU . 30200 1 75 . PRO . 30200 1 76 . TYR . 30200 1 77 . ASP . 30200 1 78 . LYS . 30200 1 79 . ARG . 30200 1 80 . LEU . 30200 1 81 . ALA . 30200 1 82 . TRP . 30200 1 83 . HIS . 30200 1 84 . PHE . 30200 1 85 . LYS . 30200 1 86 . GLU . 30200 1 87 . PHE . 30200 1 88 . CYS . 30200 1 89 . TYR . 30200 1 90 . LYS . 30200 1 91 . THR . 30200 1 92 . SER . 30200 1 93 . ALA . 30200 1 94 . HIS . 30200 1 95 . GLY . 30200 1 96 . ILE . 30200 1 97 . PRO . 30200 1 98 . MET . 30200 1 99 . ILE . 30200 1 100 . GLY . 30200 1 101 . GLU . 30200 1 102 . ALA . 30200 1 103 . PRO . 30200 1 104 . LEU . 30200 1 105 . GLU . 30200 1 106 . HIS . 30200 1 107 . HIS . 30200 1 108 . HIS . 30200 1 109 . HIS . 30200 1 110 . HIS . 30200 1 111 . HIS . 30200 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 30200 1 . SER 2 2 30200 1 . TRP 3 3 30200 1 . MET 4 4 30200 1 . GLN 5 5 30200 1 . ASN 6 6 30200 1 . LEU 7 7 30200 1 . LYS 8 8 30200 1 . ASN 9 9 30200 1 . TYR 10 10 30200 1 . GLN 11 11 30200 1 . HIS 12 12 30200 1 . LEU 13 13 30200 1 . ARG 14 14 30200 1 . ASP 15 15 30200 1 . PRO 16 16 30200 1 . SER 17 17 30200 1 . GLU 18 18 30200 1 . TYR 19 19 30200 1 . MET 20 20 30200 1 . SER 21 21 30200 1 . GLN 22 22 30200 1 . VAL 23 23 30200 1 . TYR 24 24 30200 1 . GLY 25 25 30200 1 . ASP 26 26 30200 1 . PRO 27 27 30200 1 . LEU 28 28 30200 1 . ALA 29 29 30200 1 . TYR 30 30 30200 1 . LEU 31 31 30200 1 . GLN 32 32 30200 1 . GLU 33 33 30200 1 . THR 34 34 30200 1 . THR 35 35 30200 1 . LYS 36 36 30200 1 . PHE 37 37 30200 1 . VAL 38 38 30200 1 . THR 39 39 30200 1 . GLU 40 40 30200 1 . ARG 41 41 30200 1 . GLU 42 42 30200 1 . TYR 43 43 30200 1 . TYR 44 44 30200 1 . GLU 45 45 30200 1 . ASP 46 46 30200 1 . PHE 47 47 30200 1 . GLY 48 48 30200 1 . TYR 49 49 30200 1 . GLY 50 50 30200 1 . GLU 51 51 30200 1 . CYS 52 52 30200 1 . PHE 53 53 30200 1 . ASN 54 54 30200 1 . SER 55 55 30200 1 . THR 56 56 30200 1 . GLU 57 57 30200 1 . SER 58 58 30200 1 . GLU 59 59 30200 1 . VAL 60 60 30200 1 . GLN 61 61 30200 1 . CYS 62 62 30200 1 . GLU 63 63 30200 1 . LEU 64 64 30200 1 . ILE 65 65 30200 1 . THR 66 66 30200 1 . GLY 67 67 30200 1 . GLU 68 68 30200 1 . PHE 69 69 30200 1 . ASP 70 70 30200 1 . PRO 71 71 30200 1 . LYS 72 72 30200 1 . LEU 73 73 30200 1 . LEU 74 74 30200 1 . PRO 75 75 30200 1 . TYR 76 76 30200 1 . ASP 77 77 30200 1 . LYS 78 78 30200 1 . ARG 79 79 30200 1 . LEU 80 80 30200 1 . ALA 81 81 30200 1 . TRP 82 82 30200 1 . HIS 83 83 30200 1 . PHE 84 84 30200 1 . LYS 85 85 30200 1 . GLU 86 86 30200 1 . PHE 87 87 30200 1 . CYS 88 88 30200 1 . TYR 89 89 30200 1 . LYS 90 90 30200 1 . THR 91 91 30200 1 . SER 92 92 30200 1 . ALA 93 93 30200 1 . HIS 94 94 30200 1 . GLY 95 95 30200 1 . ILE 96 96 30200 1 . PRO 97 97 30200 1 . MET 98 98 30200 1 . ILE 99 99 30200 1 . GLY 100 100 30200 1 . GLU 101 101 30200 1 . ALA 102 102 30200 1 . PRO 103 103 30200 1 . LEU 104 104 30200 1 . GLU 105 105 30200 1 . HIS 106 106 30200 1 . HIS 107 107 30200 1 . HIS 108 108 30200 1 . HIS 109 109 30200 1 . HIS 110 110 30200 1 . HIS 111 111 30200 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 30200 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity_1 . 6239 organism . 'Caenorhabditis elegans' 'C. elegans' . . Eukaryota Metazoa Caenorhabditis elegans . . . . . . . . . . . 'mec-4, mec-13, T01C8.7' . 30200 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 30200 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity_1 . 'recombinant technology' 'Escherichia coli' . . 562 Escherichia coli . . . . . . . . . . 30200 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 30200 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; 1.5 mM [U-13C; U-15N; U-2H] micelle-solubilized cytosolic amino terminal domain of C. elegans mechanosensory ion channel MEC-4, 95% H2O/5% D2O ; _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Degenerin mec-4' '[U-13C; U-15N; U-2H]' . . 1 $entity_1 . . 1.5 . . mM . . . . 30200 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 30200 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.025 . M 30200 1 pH 6.8 . pH 30200 1 pressure 1 . atm 30200 1 temperature 300 . K 30200 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 30200 _Software.ID 1 _Software.Name AutoAssign _Software.Version 2.4.0 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Zimmerman, Moseley, Kulikowski and Montelione' . . 30200 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 30200 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 30200 _Software.ID 2 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 30200 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 30200 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 30200 _Software.ID 3 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 30200 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure calculation' 30200 3 stop_ save_ save_software_4 _Software.Sf_category software _Software.Sf_framecode software_4 _Software.Entry_ID 30200 _Software.ID 4 _Software.Name 'Restrained Rosetta' _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Mao, Baker, Montelione' . . 30200 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 30200 4 stop_ save_ save_software_5 _Software.Sf_category software _Software.Sf_framecode software_5 _Software.Entry_ID 30200 _Software.ID 5 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 30200 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 30200 5 stop_ save_ save_software_6 _Software.Sf_category software _Software.Sf_framecode software_6 _Software.Entry_ID 30200 _Software.ID 6 _Software.Name TALOS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 30200 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 30200 6 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 30200 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 30200 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker Avance . 800 . . . 30200 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 30200 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 2 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 4 '3D HNCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 5 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 6 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30200 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_1 _Chem_shift_reference.Entry_ID 30200 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.000 internal indirect 0.25144953 . . . . . 30200 1 H 1 DSS 'methyl protons' . . . . ppm 0.000 internal direct 1.0 . . . . . 30200 1 N 15 DSS 'methyl protons' . . . . ppm 0.000 internal indirect 0.10132912 . . . . . 30200 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 30200 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.2 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 30200 1 2 '3D HNCO' . . . 30200 1 3 '3D HNCA' . . . 30200 1 4 '3D HNCACO' . . . 30200 1 5 '3D HN(CO)CA' . . . 30200 1 6 '2D 1H-1H NOESY' . . . 30200 1 7 '3D 1H-15N NOESY' . . . 30200 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 3 3 TRP C C 13 177.501 0.2 . . . . . A 3 TRP C . 30200 1 2 . 1 1 3 3 TRP CA C 13 59.083 0.2 . . . . . A 3 TRP CA . 30200 1 3 . 1 1 3 3 TRP CB C 13 28.036 0.2 . . . . . A 3 TRP CB . 30200 1 4 . 1 1 4 4 MET H H 1 7.908 0.02 . . . . . A 4 MET H . 30200 1 5 . 1 1 4 4 MET C C 13 177.356 0.2 . . . . . A 4 MET C . 30200 1 6 . 1 1 4 4 MET CA C 13 57.001 0.2 . . . . . A 4 MET CA . 30200 1 7 . 1 1 4 4 MET CB C 13 31.156 0.2 . . . . . A 4 MET CB . 30200 1 8 . 1 1 4 4 MET N N 15 118.436 0.2 . . . . . A 4 MET N . 30200 1 9 . 1 1 5 5 GLN H H 1 7.645 0.02 . . . . . A 5 GLN H . 30200 1 10 . 1 1 5 5 GLN C C 13 176.903 0.2 . . . . . A 5 GLN C . 30200 1 11 . 1 1 5 5 GLN CA C 13 57.090 0.2 . . . . . A 5 GLN CA . 30200 1 12 . 1 1 5 5 GLN CB C 13 27.893 0.2 . . . . . A 5 GLN CB . 30200 1 13 . 1 1 5 5 GLN N N 15 118.538 0.2 . . . . . A 5 GLN N . 30200 1 14 . 1 1 6 6 ASN H H 1 7.856 0.02 . . . . . A 6 ASN H . 30200 1 15 . 1 1 6 6 ASN C C 13 175.861 0.2 . . . . . A 6 ASN C . 30200 1 16 . 1 1 6 6 ASN CA C 13 54.029 0.2 . . . . . A 6 ASN CA . 30200 1 17 . 1 1 6 6 ASN CB C 13 38.321 0.2 . . . . . A 6 ASN CB . 30200 1 18 . 1 1 6 6 ASN N N 15 116.857 0.2 . . . . . A 6 ASN N . 30200 1 19 . 1 1 7 7 LEU H H 1 7.775 0.02 . . . . . A 7 LEU H . 30200 1 20 . 1 1 7 7 LEU C C 13 177.523 0.2 . . . . . A 7 LEU C . 30200 1 21 . 1 1 7 7 LEU CA C 13 55.808 0.2 . . . . . A 7 LEU CA . 30200 1 22 . 1 1 7 7 LEU CB C 13 40.752 0.2 . . . . . A 7 LEU CB . 30200 1 23 . 1 1 7 7 LEU N N 15 120.814 0.2 . . . . . A 7 LEU N . 30200 1 24 . 1 1 8 8 LYS H H 1 7.828 0.02 . . . . . A 8 LYS H . 30200 1 25 . 1 1 8 8 LYS C C 13 177.114 0.2 . . . . . A 8 LYS C . 30200 1 26 . 1 1 8 8 LYS CA C 13 57.746 0.2 . . . . . A 8 LYS CA . 30200 1 27 . 1 1 8 8 LYS CB C 13 31.537 0.2 . . . . . A 8 LYS CB . 30200 1 28 . 1 1 8 8 LYS N N 15 119.354 0.2 . . . . . A 8 LYS N . 30200 1 29 . 1 1 9 9 ASN H H 1 7.980 0.02 . . . . . A 9 ASN H . 30200 1 30 . 1 1 9 9 ASN C C 13 175.576 0.2 . . . . . A 9 ASN C . 30200 1 31 . 1 1 9 9 ASN CA C 13 53.351 0.2 . . . . . A 9 ASN CA . 30200 1 32 . 1 1 9 9 ASN CB C 13 37.794 0.2 . . . . . A 9 ASN CB . 30200 1 33 . 1 1 9 9 ASN N N 15 116.374 0.2 . . . . . A 9 ASN N . 30200 1 34 . 1 1 10 10 TYR H H 1 7.813 0.02 . . . . . A 10 TYR H . 30200 1 35 . 1 1 10 10 TYR C C 13 175.999 0.2 . . . . . A 10 TYR C . 30200 1 36 . 1 1 10 10 TYR CA C 13 58.611 0.2 . . . . . A 10 TYR CA . 30200 1 37 . 1 1 10 10 TYR CB C 13 37.609 0.2 . . . . . A 10 TYR CB . 30200 1 38 . 1 1 10 10 TYR N N 15 120.076 0.2 . . . . . A 10 TYR N . 30200 1 39 . 1 1 11 11 GLN H H 1 7.980 0.02 . . . . . A 11 GLN H . 30200 1 40 . 1 1 11 11 GLN C C 13 175.847 0.2 . . . . . A 11 GLN C . 30200 1 41 . 1 1 11 11 GLN CA C 13 56.888 0.2 . . . . . A 11 GLN CA . 30200 1 42 . 1 1 11 11 GLN CB C 13 27.907 0.2 . . . . . A 11 GLN CB . 30200 1 43 . 1 1 11 11 GLN N N 15 118.877 0.2 . . . . . A 11 GLN N . 30200 1 44 . 1 1 12 12 HIS H H 1 7.752 0.02 . . . . . A 12 HIS H . 30200 1 45 . 1 1 12 12 HIS C C 13 175.226 0.2 . . . . . A 12 HIS C . 30200 1 46 . 1 1 12 12 HIS CA C 13 55.641 0.2 . . . . . A 12 HIS CA . 30200 1 47 . 1 1 12 12 HIS CB C 13 29.770 0.2 . . . . . A 12 HIS CB . 30200 1 48 . 1 1 12 12 HIS N N 15 116.944 0.2 . . . . . A 12 HIS N . 30200 1 49 . 1 1 13 13 LEU H H 1 7.521 0.02 . . . . . A 13 LEU H . 30200 1 50 . 1 1 13 13 LEU C C 13 176.264 0.2 . . . . . A 13 LEU C . 30200 1 51 . 1 1 13 13 LEU CA C 13 54.593 0.2 . . . . . A 13 LEU CA . 30200 1 52 . 1 1 13 13 LEU CB C 13 41.394 0.2 . . . . . A 13 LEU CB . 30200 1 53 . 1 1 13 13 LEU N N 15 121.435 0.2 . . . . . A 13 LEU N . 30200 1 54 . 1 1 14 14 ARG H H 1 7.880 0.02 . . . . . A 14 ARG H . 30200 1 55 . 1 1 14 14 ARG C C 13 175.576 0.2 . . . . . A 14 ARG C . 30200 1 56 . 1 1 14 14 ARG CA C 13 55.477 0.2 . . . . . A 14 ARG CA . 30200 1 57 . 1 1 14 14 ARG CB C 13 30.213 0.2 . . . . . A 14 ARG CB . 30200 1 58 . 1 1 14 14 ARG N N 15 120.839 0.2 . . . . . A 14 ARG N . 30200 1 59 . 1 1 15 15 ASP H H 1 8.300 0.02 . . . . . A 15 ASP H . 30200 1 60 . 1 1 15 15 ASP CA C 13 51.914 0.2 . . . . . A 15 ASP CA . 30200 1 61 . 1 1 15 15 ASP CB C 13 41.036 0.2 . . . . . A 15 ASP CB . 30200 1 62 . 1 1 15 15 ASP N N 15 120.013 0.2 . . . . . A 15 ASP N . 30200 1 63 . 1 1 16 16 PRO C C 13 177.220 0.2 . . . . . A 16 PRO C . 30200 1 64 . 1 1 16 16 PRO CA C 13 63.751 0.2 . . . . . A 16 PRO CA . 30200 1 65 . 1 1 16 16 PRO CB C 13 31.049 0.2 . . . . . A 16 PRO CB . 30200 1 66 . 1 1 17 17 SER H H 1 8.525 0.02 . . . . . A 17 SER H . 30200 1 67 . 1 1 17 17 SER C C 13 176.052 0.2 . . . . . A 17 SER C . 30200 1 68 . 1 1 17 17 SER CA C 13 61.480 0.2 . . . . . A 17 SER CA . 30200 1 69 . 1 1 17 17 SER CB C 13 62.172 0.2 . . . . . A 17 SER CB . 30200 1 70 . 1 1 17 17 SER N N 15 115.950 0.2 . . . . . A 17 SER N . 30200 1 71 . 1 1 18 18 GLU H H 1 8.150 0.02 . . . . . A 18 GLU H . 30200 1 72 . 1 1 18 18 GLU C C 13 178.066 0.2 . . . . . A 18 GLU C . 30200 1 73 . 1 1 18 18 GLU CA C 13 58.112 0.2 . . . . . A 18 GLU CA . 30200 1 74 . 1 1 18 18 GLU CB C 13 28.547 0.2 . . . . . A 18 GLU CB . 30200 1 75 . 1 1 18 18 GLU N N 15 122.413 0.2 . . . . . A 18 GLU N . 30200 1 76 . 1 1 19 19 TYR H H 1 7.717 0.02 . . . . . A 19 TYR H . 30200 1 77 . 1 1 19 19 TYR C C 13 177.155 0.2 . . . . . A 19 TYR C . 30200 1 78 . 1 1 19 19 TYR CA C 13 59.222 0.2 . . . . . A 19 TYR CA . 30200 1 79 . 1 1 19 19 TYR CB C 13 37.809 0.2 . . . . . A 19 TYR CB . 30200 1 80 . 1 1 19 19 TYR N N 15 118.768 0.2 . . . . . A 19 TYR N . 30200 1 81 . 1 1 20 20 MET H H 1 7.950 0.02 . . . . . A 20 MET H . 30200 1 82 . 1 1 20 20 MET C C 13 177.334 0.2 . . . . . A 20 MET C . 30200 1 83 . 1 1 20 20 MET CA C 13 56.774 0.2 . . . . . A 20 MET CA . 30200 1 84 . 1 1 20 20 MET CB C 13 31.317 0.2 . . . . . A 20 MET CB . 30200 1 85 . 1 1 20 20 MET N N 15 117.327 0.2 . . . . . A 20 MET N . 30200 1 86 . 1 1 21 21 SER H H 1 7.952 0.02 . . . . . A 21 SER H . 30200 1 87 . 1 1 21 21 SER C C 13 176.046 0.2 . . . . . A 21 SER C . 30200 1 88 . 1 1 21 21 SER CA C 13 60.423 0.2 . . . . . A 21 SER CA . 30200 1 89 . 1 1 21 21 SER CB C 13 62.272 0.2 . . . . . A 21 SER CB . 30200 1 90 . 1 1 21 21 SER N N 15 114.597 0.2 . . . . . A 21 SER N . 30200 1 91 . 1 1 22 22 GLN H H 1 7.860 0.02 . . . . . A 22 GLN H . 30200 1 92 . 1 1 22 22 GLN C C 13 177.198 0.2 . . . . . A 22 GLN C . 30200 1 93 . 1 1 22 22 GLN CA C 13 57.022 0.2 . . . . . A 22 GLN CA . 30200 1 94 . 1 1 22 22 GLN CB C 13 27.821 0.2 . . . . . A 22 GLN CB . 30200 1 95 . 1 1 22 22 GLN N N 15 120.999 0.2 . . . . . A 22 GLN N . 30200 1 96 . 1 1 23 23 VAL H H 1 7.479 0.02 . . . . . A 23 VAL H . 30200 1 97 . 1 1 23 23 VAL C C 13 175.721 0.2 . . . . . A 23 VAL C . 30200 1 98 . 1 1 23 23 VAL CA C 13 63.623 0.2 . . . . . A 23 VAL CA . 30200 1 99 . 1 1 23 23 VAL CB C 13 31.346 0.2 . . . . . A 23 VAL CB . 30200 1 100 . 1 1 23 23 VAL N N 15 118.510 0.2 . . . . . A 23 VAL N . 30200 1 101 . 1 1 24 24 TYR H H 1 7.689 0.02 . . . . . A 24 TYR H . 30200 1 102 . 1 1 24 24 TYR C C 13 175.719 0.2 . . . . . A 24 TYR C . 30200 1 103 . 1 1 24 24 TYR CA C 13 58.580 0.2 . . . . . A 24 TYR CA . 30200 1 104 . 1 1 24 24 TYR CB C 13 38.148 0.2 . . . . . A 24 TYR CB . 30200 1 105 . 1 1 24 24 TYR N N 15 118.494 0.2 . . . . . A 24 TYR N . 30200 1 106 . 1 1 25 25 GLY H H 1 7.694 0.02 . . . . . A 25 GLY H . 30200 1 107 . 1 1 25 25 GLY C C 13 173.688 0.2 . . . . . A 25 GLY C . 30200 1 108 . 1 1 25 25 GLY CA C 13 45.353 0.2 . . . . . A 25 GLY CA . 30200 1 109 . 1 1 25 25 GLY N N 15 105.596 0.2 . . . . . A 25 GLY N . 30200 1 110 . 1 1 26 26 ASP H H 1 7.790 0.02 . . . . . A 26 ASP H . 30200 1 111 . 1 1 26 26 ASP CA C 13 51.771 0.2 . . . . . A 26 ASP CA . 30200 1 112 . 1 1 26 26 ASP CB C 13 40.239 0.2 . . . . . A 26 ASP CB . 30200 1 113 . 1 1 26 26 ASP N N 15 118.611 0.2 . . . . . A 26 ASP N . 30200 1 114 . 1 1 27 27 PRO C C 13 178.412 0.2 . . . . . A 27 PRO C . 30200 1 115 . 1 1 27 27 PRO CA C 13 64.716 0.2 . . . . . A 27 PRO CA . 30200 1 116 . 1 1 27 27 PRO CB C 13 31.334 0.2 . . . . . A 27 PRO CB . 30200 1 117 . 1 1 28 28 LEU H H 1 8.250 0.02 . . . . . A 28 LEU H . 30200 1 118 . 1 1 28 28 LEU C C 13 179.045 0.2 . . . . . A 28 LEU C . 30200 1 119 . 1 1 28 28 LEU CA C 13 57.172 0.2 . . . . . A 28 LEU CA . 30200 1 120 . 1 1 28 28 LEU CB C 13 39.527 0.2 . . . . . A 28 LEU CB . 30200 1 121 . 1 1 28 28 LEU N N 15 117.304 0.2 . . . . . A 28 LEU N . 30200 1 122 . 1 1 29 29 ALA H H 1 7.584 0.02 . . . . . A 29 ALA H . 30200 1 123 . 1 1 29 29 ALA C C 13 180.143 0.2 . . . . . A 29 ALA C . 30200 1 124 . 1 1 29 29 ALA CA C 13 54.204 0.2 . . . . . A 29 ALA CA . 30200 1 125 . 1 1 29 29 ALA CB C 13 17.361 0.2 . . . . . A 29 ALA CB . 30200 1 126 . 1 1 29 29 ALA N N 15 122.659 0.2 . . . . . A 29 ALA N . 30200 1 127 . 1 1 30 30 TYR H H 1 7.611 0.02 . . . . . A 30 TYR H . 30200 1 128 . 1 1 30 30 TYR C C 13 178.334 0.2 . . . . . A 30 TYR C . 30200 1 129 . 1 1 30 30 TYR CA C 13 60.324 0.2 . . . . . A 30 TYR CA . 30200 1 130 . 1 1 30 30 TYR CB C 13 37.765 0.2 . . . . . A 30 TYR CB . 30200 1 131 . 1 1 30 30 TYR N N 15 117.638 0.2 . . . . . A 30 TYR N . 30200 1 132 . 1 1 31 31 LEU H H 1 8.144 0.02 . . . . . A 31 LEU H . 30200 1 133 . 1 1 31 31 LEU C C 13 178.857 0.2 . . . . . A 31 LEU C . 30200 1 134 . 1 1 31 31 LEU CA C 13 56.935 0.2 . . . . . A 31 LEU CA . 30200 1 135 . 1 1 31 31 LEU CB C 13 41.041 0.2 . . . . . A 31 LEU CB . 30200 1 136 . 1 1 31 31 LEU N N 15 120.733 0.2 . . . . . A 31 LEU N . 30200 1 137 . 1 1 32 32 GLN H H 1 8.259 0.02 . . . . . A 32 GLN H . 30200 1 138 . 1 1 32 32 GLN C C 13 177.753 0.2 . . . . . A 32 GLN C . 30200 1 139 . 1 1 32 32 GLN CA C 13 58.461 0.2 . . . . . A 32 GLN CA . 30200 1 140 . 1 1 32 32 GLN CB C 13 27.839 0.2 . . . . . A 32 GLN CB . 30200 1 141 . 1 1 32 32 GLN N N 15 120.229 0.2 . . . . . A 32 GLN N . 30200 1 142 . 1 1 33 33 GLU H H 1 8.031 0.02 . . . . . A 33 GLU H . 30200 1 143 . 1 1 33 33 GLU C C 13 178.527 0.2 . . . . . A 33 GLU C . 30200 1 144 . 1 1 33 33 GLU CA C 13 57.960 0.2 . . . . . A 33 GLU CA . 30200 1 145 . 1 1 33 33 GLU CB C 13 28.820 0.2 . . . . . A 33 GLU CB . 30200 1 146 . 1 1 33 33 GLU N N 15 119.369 0.2 . . . . . A 33 GLU N . 30200 1 147 . 1 1 34 34 THR H H 1 7.885 0.02 . . . . . A 34 THR H . 30200 1 148 . 1 1 34 34 THR C C 13 175.744 0.2 . . . . . A 34 THR C . 30200 1 149 . 1 1 34 34 THR CA C 13 65.018 0.2 . . . . . A 34 THR CA . 30200 1 150 . 1 1 34 34 THR CB C 13 68.361 0.2 . . . . . A 34 THR CB . 30200 1 151 . 1 1 34 34 THR N N 15 113.837 0.2 . . . . . A 34 THR N . 30200 1 152 . 1 1 35 35 THR H H 1 7.734 0.02 . . . . . A 35 THR H . 30200 1 153 . 1 1 35 35 THR C C 13 175.641 0.2 . . . . . A 35 THR C . 30200 1 154 . 1 1 35 35 THR CA C 13 63.933 0.2 . . . . . A 35 THR CA . 30200 1 155 . 1 1 35 35 THR CB C 13 68.367 0.2 . . . . . A 35 THR CB . 30200 1 156 . 1 1 35 35 THR N N 15 113.018 0.2 . . . . . A 35 THR N . 30200 1 157 . 1 1 36 36 LYS H H 1 7.563 0.02 . . . . . A 36 LYS H . 30200 1 158 . 1 1 36 36 LYS C C 13 176.985 0.2 . . . . . A 36 LYS C . 30200 1 159 . 1 1 36 36 LYS CA C 13 57.925 0.2 . . . . . A 36 LYS CA . 30200 1 160 . 1 1 36 36 LYS CB C 13 31.230 0.2 . . . . . A 36 LYS CB . 30200 1 161 . 1 1 36 36 LYS N N 15 122.248 0.2 . . . . . A 36 LYS N . 30200 1 162 . 1 1 37 37 PHE H H 1 7.770 0.02 . . . . . A 37 PHE H . 30200 1 163 . 1 1 37 37 PHE C C 13 175.938 0.2 . . . . . A 37 PHE C . 30200 1 164 . 1 1 37 37 PHE CA C 13 58.451 0.2 . . . . . A 37 PHE CA . 30200 1 165 . 1 1 37 37 PHE CB C 13 38.503 0.2 . . . . . A 37 PHE CB . 30200 1 166 . 1 1 37 37 PHE N N 15 117.915 0.2 . . . . . A 37 PHE N . 30200 1 167 . 1 1 38 38 VAL H H 1 7.657 0.02 . . . . . A 38 VAL H . 30200 1 168 . 1 1 38 38 VAL C C 13 175.877 0.2 . . . . . A 38 VAL C . 30200 1 169 . 1 1 38 38 VAL CA C 13 62.769 0.2 . . . . . A 38 VAL CA . 30200 1 170 . 1 1 38 38 VAL CB C 13 31.848 0.2 . . . . . A 38 VAL CB . 30200 1 171 . 1 1 38 38 VAL N N 15 117.220 0.2 . . . . . A 38 VAL N . 30200 1 172 . 1 1 39 39 THR H H 1 7.928 0.02 . . . . . A 39 THR H . 30200 1 173 . 1 1 39 39 THR C C 13 175.058 0.2 . . . . . A 39 THR C . 30200 1 174 . 1 1 39 39 THR CA C 13 61.721 0.2 . . . . . A 39 THR CA . 30200 1 175 . 1 1 39 39 THR CB C 13 69.480 0.2 . . . . . A 39 THR CB . 30200 1 176 . 1 1 39 39 THR N N 15 113.454 0.2 . . . . . A 39 THR N . 30200 1 177 . 1 1 40 40 GLU H H 1 8.219 0.02 . . . . . A 40 GLU H . 30200 1 178 . 1 1 40 40 GLU CA C 13 57.133 0.2 . . . . . A 40 GLU CA . 30200 1 179 . 1 1 40 40 GLU N N 15 121.953 0.2 . . . . . A 40 GLU N . 30200 1 180 . 1 1 43 43 TYR C C 13 175.595 0.2 . . . . . A 43 TYR C . 30200 1 181 . 1 1 43 43 TYR CA C 13 58.886 0.2 . . . . . A 43 TYR CA . 30200 1 182 . 1 1 43 43 TYR CB C 13 37.989 0.2 . . . . . A 43 TYR CB . 30200 1 183 . 1 1 44 44 TYR H H 1 7.578 0.02 . . . . . A 44 TYR H . 30200 1 184 . 1 1 44 44 TYR C C 13 176.179 0.2 . . . . . A 44 TYR C . 30200 1 185 . 1 1 44 44 TYR CA C 13 58.193 0.2 . . . . . A 44 TYR CA . 30200 1 186 . 1 1 44 44 TYR CB C 13 37.734 0.2 . . . . . A 44 TYR CB . 30200 1 187 . 1 1 44 44 TYR N N 15 116.896 0.2 . . . . . A 44 TYR N . 30200 1 188 . 1 1 45 45 GLU H H 1 7.835 0.02 . . . . . A 45 GLU H . 30200 1 189 . 1 1 45 45 GLU C C 13 176.427 0.2 . . . . . A 45 GLU C . 30200 1 190 . 1 1 45 45 GLU CA C 13 57.115 0.2 . . . . . A 45 GLU CA . 30200 1 191 . 1 1 45 45 GLU CB C 13 29.348 0.2 . . . . . A 45 GLU CB . 30200 1 192 . 1 1 45 45 GLU N N 15 121.033 0.2 . . . . . A 45 GLU N . 30200 1 193 . 1 1 46 46 ASP H H 1 8.024 0.02 . . . . . A 46 ASP H . 30200 1 194 . 1 1 46 46 ASP C C 13 176.235 0.2 . . . . . A 46 ASP C . 30200 1 195 . 1 1 46 46 ASP CA C 13 54.257 0.2 . . . . . A 46 ASP CA . 30200 1 196 . 1 1 46 46 ASP CB C 13 40.502 0.2 . . . . . A 46 ASP CB . 30200 1 197 . 1 1 46 46 ASP N N 15 119.204 0.2 . . . . . A 46 ASP N . 30200 1 198 . 1 1 47 47 PHE H H 1 7.864 0.02 . . . . . A 47 PHE H . 30200 1 199 . 1 1 47 47 PHE C C 13 175.141 0.2 . . . . . A 47 PHE C . 30200 1 200 . 1 1 47 47 PHE CA C 13 57.723 0.2 . . . . . A 47 PHE CA . 30200 1 201 . 1 1 47 47 PHE CB C 13 38.223 0.2 . . . . . A 47 PHE CB . 30200 1 202 . 1 1 47 47 PHE N N 15 118.989 0.2 . . . . . A 47 PHE N . 30200 1 203 . 1 1 48 48 GLY H H 1 7.976 0.02 . . . . . A 48 GLY H . 30200 1 204 . 1 1 48 48 GLY C C 13 174.566 0.2 . . . . . A 48 GLY C . 30200 1 205 . 1 1 48 48 GLY CA C 13 45.232 0.2 . . . . . A 48 GLY CA . 30200 1 206 . 1 1 48 48 GLY N N 15 107.284 0.2 . . . . . A 48 GLY N . 30200 1 207 . 1 1 49 49 TYR H H 1 7.928 0.02 . . . . . A 49 TYR H . 30200 1 208 . 1 1 49 49 TYR C C 13 176.599 0.2 . . . . . A 49 TYR C . 30200 1 209 . 1 1 49 49 TYR CA C 13 58.724 0.2 . . . . . A 49 TYR CA . 30200 1 210 . 1 1 49 49 TYR CB C 13 37.798 0.2 . . . . . A 49 TYR CB . 30200 1 211 . 1 1 49 49 TYR N N 15 119.694 0.2 . . . . . A 49 TYR N . 30200 1 212 . 1 1 50 50 GLY H H 1 8.482 0.02 . . . . . A 50 GLY H . 30200 1 213 . 1 1 50 50 GLY C C 13 175.087 0.2 . . . . . A 50 GLY C . 30200 1 214 . 1 1 50 50 GLY CA C 13 45.846 0.2 . . . . . A 50 GLY CA . 30200 1 215 . 1 1 50 50 GLY N N 15 108.779 0.2 . . . . . A 50 GLY N . 30200 1 216 . 1 1 51 51 GLU H H 1 8.222 0.02 . . . . . A 51 GLU H . 30200 1 217 . 1 1 51 51 GLU C C 13 177.502 0.2 . . . . . A 51 GLU C . 30200 1 218 . 1 1 51 51 GLU CA C 13 56.968 0.2 . . . . . A 51 GLU CA . 30200 1 219 . 1 1 51 51 GLU CB C 13 28.827 0.2 . . . . . A 51 GLU CB . 30200 1 220 . 1 1 51 51 GLU N N 15 120.567 0.2 . . . . . A 51 GLU N . 30200 1 221 . 1 1 52 52 CYS H H 1 7.931 0.02 . . . . . A 52 CYS H . 30200 1 222 . 1 1 52 52 CYS C C 13 174.359 0.2 . . . . . A 52 CYS C . 30200 1 223 . 1 1 52 52 CYS CA C 13 59.794 0.2 . . . . . A 52 CYS CA . 30200 1 224 . 1 1 52 52 CYS CB C 13 27.236 0.2 . . . . . A 52 CYS CB . 30200 1 225 . 1 1 52 52 CYS N N 15 117.587 0.2 . . . . . A 52 CYS N . 30200 1 226 . 1 1 53 53 PHE H H 1 7.926 0.02 . . . . . A 53 PHE H . 30200 1 227 . 1 1 53 53 PHE C C 13 175.084 0.2 . . . . . A 53 PHE C . 30200 1 228 . 1 1 53 53 PHE CA C 13 57.402 0.2 . . . . . A 53 PHE CA . 30200 1 229 . 1 1 53 53 PHE CB C 13 38.512 0.2 . . . . . A 53 PHE CB . 30200 1 230 . 1 1 53 53 PHE N N 15 118.506 0.2 . . . . . A 53 PHE N . 30200 1 231 . 1 1 54 54 ASN H H 1 7.992 0.02 . . . . . A 54 ASN H . 30200 1 232 . 1 1 54 54 ASN C C 13 175.284 0.2 . . . . . A 54 ASN C . 30200 1 233 . 1 1 54 54 ASN CA C 13 52.889 0.2 . . . . . A 54 ASN CA . 30200 1 234 . 1 1 54 54 ASN CB C 13 38.479 0.2 . . . . . A 54 ASN CB . 30200 1 235 . 1 1 54 54 ASN N N 15 119.285 0.2 . . . . . A 54 ASN N . 30200 1 236 . 1 1 55 55 SER H H 1 8.176 0.02 . . . . . A 55 SER H . 30200 1 237 . 1 1 55 55 SER C C 13 174.928 0.2 . . . . . A 55 SER C . 30200 1 238 . 1 1 55 55 SER CA C 13 58.042 0.2 . . . . . A 55 SER CA . 30200 1 239 . 1 1 55 55 SER CB C 13 63.368 0.2 . . . . . A 55 SER CB . 30200 1 240 . 1 1 55 55 SER N N 15 116.602 0.2 . . . . . A 55 SER N . 30200 1 241 . 1 1 56 56 THR H H 1 8.252 0.02 . . . . . A 56 THR H . 30200 1 242 . 1 1 56 56 THR C C 13 175.005 0.2 . . . . . A 56 THR C . 30200 1 243 . 1 1 56 56 THR CA C 13 62.052 0.2 . . . . . A 56 THR CA . 30200 1 244 . 1 1 56 56 THR CB C 13 69.019 0.2 . . . . . A 56 THR CB . 30200 1 245 . 1 1 56 56 THR N N 15 116.474 0.2 . . . . . A 56 THR N . 30200 1 246 . 1 1 57 57 GLU H H 1 8.392 0.02 . . . . . A 57 GLU H . 30200 1 247 . 1 1 57 57 GLU C C 13 176.875 0.2 . . . . . A 57 GLU C . 30200 1 248 . 1 1 57 57 GLU CA C 13 56.789 0.2 . . . . . A 57 GLU CA . 30200 1 249 . 1 1 57 57 GLU CB C 13 29.169 0.2 . . . . . A 57 GLU CB . 30200 1 250 . 1 1 57 57 GLU N N 15 122.826 0.2 . . . . . A 57 GLU N . 30200 1 251 . 1 1 58 58 SER H H 1 8.149 0.02 . . . . . A 58 SER H . 30200 1 252 . 1 1 58 58 SER C C 13 174.807 0.2 . . . . . A 58 SER C . 30200 1 253 . 1 1 58 58 SER CA C 13 58.590 0.2 . . . . . A 58 SER CA . 30200 1 254 . 1 1 58 58 SER CB C 13 63.040 0.2 . . . . . A 58 SER CB . 30200 1 255 . 1 1 58 58 SER N N 15 116.315 0.2 . . . . . A 58 SER N . 30200 1 256 . 1 1 59 59 GLU H H 1 8.256 0.02 . . . . . A 59 GLU H . 30200 1 257 . 1 1 59 59 GLU C C 13 176.885 0.2 . . . . . A 59 GLU C . 30200 1 258 . 1 1 59 59 GLU CA C 13 56.723 0.2 . . . . . A 59 GLU CA . 30200 1 259 . 1 1 59 59 GLU CB C 13 29.325 0.2 . . . . . A 59 GLU CB . 30200 1 260 . 1 1 59 59 GLU N N 15 123.043 0.2 . . . . . A 59 GLU N . 30200 1 261 . 1 1 60 60 VAL H H 1 8.008 0.02 . . . . . A 60 VAL H . 30200 1 262 . 1 1 60 60 VAL C C 13 176.174 0.2 . . . . . A 60 VAL C . 30200 1 263 . 1 1 60 60 VAL CA C 13 62.468 0.2 . . . . . A 60 VAL CA . 30200 1 264 . 1 1 60 60 VAL CB C 13 32.032 0.2 . . . . . A 60 VAL CB . 30200 1 265 . 1 1 60 60 VAL N N 15 120.903 0.2 . . . . . A 60 VAL N . 30200 1 266 . 1 1 61 61 GLN H H 1 8.235 0.02 . . . . . A 61 GLN H . 30200 1 267 . 1 1 61 61 GLN C C 13 176.219 0.2 . . . . . A 61 GLN C . 30200 1 268 . 1 1 61 61 GLN CA C 13 55.732 0.2 . . . . . A 61 GLN CA . 30200 1 269 . 1 1 61 61 GLN CB C 13 28.322 0.2 . . . . . A 61 GLN CB . 30200 1 270 . 1 1 61 61 GLN N N 15 123.484 0.2 . . . . . A 61 GLN N . 30200 1 271 . 1 1 62 62 CYS H H 1 8.319 0.02 . . . . . A 62 CYS H . 30200 1 272 . 1 1 62 62 CYS C C 13 174.910 0.2 . . . . . A 62 CYS C . 30200 1 273 . 1 1 62 62 CYS CA C 13 59.177 0.2 . . . . . A 62 CYS CA . 30200 1 274 . 1 1 62 62 CYS CB C 13 27.299 0.2 . . . . . A 62 CYS CB . 30200 1 275 . 1 1 62 62 CYS N N 15 120.482 0.2 . . . . . A 62 CYS N . 30200 1 276 . 1 1 63 63 GLU H H 1 8.549 0.02 . . . . . A 63 GLU H . 30200 1 277 . 1 1 63 63 GLU C C 13 176.807 0.2 . . . . . A 63 GLU C . 30200 1 278 . 1 1 63 63 GLU CA C 13 57.006 0.2 . . . . . A 63 GLU CA . 30200 1 279 . 1 1 63 63 GLU CB C 13 29.011 0.2 . . . . . A 63 GLU CB . 30200 1 280 . 1 1 63 63 GLU N N 15 123.519 0.2 . . . . . A 63 GLU N . 30200 1 281 . 1 1 64 64 LEU H H 1 8.021 0.02 . . . . . A 64 LEU H . 30200 1 282 . 1 1 64 64 LEU C C 13 177.095 0.2 . . . . . A 64 LEU C . 30200 1 283 . 1 1 64 64 LEU CA C 13 55.507 0.2 . . . . . A 64 LEU CA . 30200 1 284 . 1 1 64 64 LEU CB C 13 41.505 0.2 . . . . . A 64 LEU CB . 30200 1 285 . 1 1 64 64 LEU N N 15 121.741 0.2 . . . . . A 64 LEU N . 30200 1 286 . 1 1 65 65 ILE H H 1 7.835 0.02 . . . . . A 65 ILE H . 30200 1 287 . 1 1 65 65 ILE C C 13 176.210 0.2 . . . . . A 65 ILE C . 30200 1 288 . 1 1 65 65 ILE CA C 13 60.982 0.2 . . . . . A 65 ILE CA . 30200 1 289 . 1 1 65 65 ILE CB C 13 37.512 0.2 . . . . . A 65 ILE CB . 30200 1 290 . 1 1 65 65 ILE N N 15 119.160 0.2 . . . . . A 65 ILE N . 30200 1 291 . 1 1 66 66 THR H H 1 7.968 0.02 . . . . . A 66 THR H . 30200 1 292 . 1 1 66 66 THR C C 13 175.364 0.2 . . . . . A 66 THR C . 30200 1 293 . 1 1 66 66 THR CA C 13 61.855 0.2 . . . . . A 66 THR CA . 30200 1 294 . 1 1 66 66 THR CB C 13 69.223 0.2 . . . . . A 66 THR CB . 30200 1 295 . 1 1 66 66 THR N N 15 114.985 0.2 . . . . . A 66 THR N . 30200 1 296 . 1 1 67 67 GLY H H 1 8.165 0.02 . . . . . A 67 GLY H . 30200 1 297 . 1 1 67 67 GLY C C 13 173.805 0.2 . . . . . A 67 GLY C . 30200 1 298 . 1 1 67 67 GLY CA C 13 44.920 0.2 . . . . . A 67 GLY CA . 30200 1 299 . 1 1 67 67 GLY N N 15 110.751 0.2 . . . . . A 67 GLY N . 30200 1 300 . 1 1 68 68 GLU H H 1 8.106 0.02 . . . . . A 68 GLU H . 30200 1 301 . 1 1 68 68 GLU C C 13 176.015 0.2 . . . . . A 68 GLU C . 30200 1 302 . 1 1 68 68 GLU CA C 13 55.906 0.2 . . . . . A 68 GLU CA . 30200 1 303 . 1 1 68 68 GLU CB C 13 29.510 0.2 . . . . . A 68 GLU CB . 30200 1 304 . 1 1 68 68 GLU N N 15 120.406 0.2 . . . . . A 68 GLU N . 30200 1 305 . 1 1 69 69 PHE H H 1 8.104 0.02 . . . . . A 69 PHE H . 30200 1 306 . 1 1 69 69 PHE C C 13 173.986 0.2 . . . . . A 69 PHE C . 30200 1 307 . 1 1 69 69 PHE CA C 13 57.150 0.2 . . . . . A 69 PHE CA . 30200 1 308 . 1 1 69 69 PHE CB C 13 39.095 0.2 . . . . . A 69 PHE CB . 30200 1 309 . 1 1 69 69 PHE N N 15 121.384 0.2 . . . . . A 69 PHE N . 30200 1 310 . 1 1 70 70 ASP H H 1 7.773 0.02 . . . . . A 70 ASP H . 30200 1 311 . 1 1 70 70 ASP CA C 13 50.482 0.2 . . . . . A 70 ASP CA . 30200 1 312 . 1 1 70 70 ASP CB C 13 41.495 0.2 . . . . . A 70 ASP CB . 30200 1 313 . 1 1 70 70 ASP N N 15 124.689 0.2 . . . . . A 70 ASP N . 30200 1 314 . 1 1 71 71 PRO C C 13 177.464 0.2 . . . . . A 71 PRO C . 30200 1 315 . 1 1 71 71 PRO CA C 13 63.463 0.2 . . . . . A 71 PRO CA . 30200 1 316 . 1 1 71 71 PRO CB C 13 31.115 0.2 . . . . . A 71 PRO CB . 30200 1 317 . 1 1 72 72 LYS H H 1 8.206 0.02 . . . . . A 72 LYS H . 30200 1 318 . 1 1 72 72 LYS C C 13 177.232 0.2 . . . . . A 72 LYS C . 30200 1 319 . 1 1 72 72 LYS CA C 13 57.517 0.2 . . . . . A 72 LYS CA . 30200 1 320 . 1 1 72 72 LYS CB C 13 30.710 0.2 . . . . . A 72 LYS CB . 30200 1 321 . 1 1 72 72 LYS N N 15 117.818 0.2 . . . . . A 72 LYS N . 30200 1 322 . 1 1 73 73 LEU H H 1 7.605 0.02 . . . . . A 73 LEU H . 30200 1 323 . 1 1 73 73 LEU C C 13 177.136 0.2 . . . . . A 73 LEU C . 30200 1 324 . 1 1 73 73 LEU CA C 13 54.339 0.2 . . . . . A 73 LEU CA . 30200 1 325 . 1 1 73 73 LEU CB C 13 41.345 0.2 . . . . . A 73 LEU CB . 30200 1 326 . 1 1 73 73 LEU N N 15 118.447 0.2 . . . . . A 73 LEU N . 30200 1 327 . 1 1 74 74 LEU H H 1 7.440 0.02 . . . . . A 74 LEU H . 30200 1 328 . 1 1 74 74 LEU CA C 13 52.716 0.2 . . . . . A 74 LEU CA . 30200 1 329 . 1 1 74 74 LEU CB C 13 41.204 0.2 . . . . . A 74 LEU CB . 30200 1 330 . 1 1 74 74 LEU N N 15 120.783 0.2 . . . . . A 74 LEU N . 30200 1 331 . 1 1 75 75 PRO C C 13 176.028 0.2 . . . . . A 75 PRO C . 30200 1 332 . 1 1 75 75 PRO CA C 13 62.081 0.2 . . . . . A 75 PRO CA . 30200 1 333 . 1 1 75 75 PRO CB C 13 33.290 0.2 . . . . . A 75 PRO CB . 30200 1 334 . 1 1 76 76 TYR H H 1 8.478 0.02 . . . . . A 76 TYR H . 30200 1 335 . 1 1 76 76 TYR C C 13 177.194 0.2 . . . . . A 76 TYR C . 30200 1 336 . 1 1 76 76 TYR CA C 13 54.919 0.2 . . . . . A 76 TYR CA . 30200 1 337 . 1 1 76 76 TYR CB C 13 41.201 0.2 . . . . . A 76 TYR CB . 30200 1 338 . 1 1 76 76 TYR N N 15 124.286 0.2 . . . . . A 76 TYR N . 30200 1 339 . 1 1 78 78 LYS C C 13 178.081 0.2 . . . . . A 78 LYS C . 30200 1 340 . 1 1 78 78 LYS CA C 13 57.734 0.2 . . . . . A 78 LYS CA . 30200 1 341 . 1 1 78 78 LYS CB C 13 31.738 0.2 . . . . . A 78 LYS CB . 30200 1 342 . 1 1 79 79 ARG H H 1 8.439 0.02 . . . . . A 79 ARG H . 30200 1 343 . 1 1 79 79 ARG C C 13 177.941 0.2 . . . . . A 79 ARG C . 30200 1 344 . 1 1 79 79 ARG CA C 13 57.844 0.2 . . . . . A 79 ARG CA . 30200 1 345 . 1 1 79 79 ARG CB C 13 29.164 0.2 . . . . . A 79 ARG CB . 30200 1 346 . 1 1 79 79 ARG N N 15 121.156 0.2 . . . . . A 79 ARG N . 30200 1 347 . 1 1 80 80 LEU H H 1 8.065 0.02 . . . . . A 80 LEU H . 30200 1 348 . 1 1 80 80 LEU C C 13 177.967 0.2 . . . . . A 80 LEU C . 30200 1 349 . 1 1 80 80 LEU CA C 13 56.981 0.2 . . . . . A 80 LEU CA . 30200 1 350 . 1 1 80 80 LEU CB C 13 40.911 0.2 . . . . . A 80 LEU CB . 30200 1 351 . 1 1 80 80 LEU N N 15 120.235 0.2 . . . . . A 80 LEU N . 30200 1 352 . 1 1 81 81 ALA H H 1 7.808 0.02 . . . . . A 81 ALA H . 30200 1 353 . 1 1 81 81 ALA C C 13 178.845 0.2 . . . . . A 81 ALA C . 30200 1 354 . 1 1 81 81 ALA CA C 13 54.273 0.2 . . . . . A 81 ALA CA . 30200 1 355 . 1 1 81 81 ALA CB C 13 17.851 0.2 . . . . . A 81 ALA CB . 30200 1 356 . 1 1 81 81 ALA N N 15 120.534 0.2 . . . . . A 81 ALA N . 30200 1 357 . 1 1 82 82 TRP H H 1 7.994 0.02 . . . . . A 82 TRP H . 30200 1 358 . 1 1 82 82 TRP C C 13 177.416 0.2 . . . . . A 82 TRP C . 30200 1 359 . 1 1 82 82 TRP CA C 13 59.667 0.2 . . . . . A 82 TRP CA . 30200 1 360 . 1 1 82 82 TRP CB C 13 28.253 0.2 . . . . . A 82 TRP CB . 30200 1 361 . 1 1 82 82 TRP N N 15 120.008 0.2 . . . . . A 82 TRP N . 30200 1 362 . 1 1 83 83 HIS C C 13 177.532 0.2 . . . . . A 83 HIS C . 30200 1 363 . 1 1 83 83 HIS CA C 13 58.437 0.2 . . . . . A 83 HIS CA . 30200 1 364 . 1 1 83 83 HIS CB C 13 29.859 0.2 . . . . . A 83 HIS CB . 30200 1 365 . 1 1 84 84 PHE H H 1 8.408 0.02 . . . . . A 84 PHE H . 30200 1 366 . 1 1 84 84 PHE C C 13 176.710 0.2 . . . . . A 84 PHE C . 30200 1 367 . 1 1 84 84 PHE CA C 13 60.035 0.2 . . . . . A 84 PHE CA . 30200 1 368 . 1 1 84 84 PHE CB C 13 38.476 0.2 . . . . . A 84 PHE CB . 30200 1 369 . 1 1 84 84 PHE N N 15 120.185 0.2 . . . . . A 84 PHE N . 30200 1 370 . 1 1 85 85 LYS H H 1 8.179 0.02 . . . . . A 85 LYS H . 30200 1 371 . 1 1 85 85 LYS C C 13 177.887 0.2 . . . . . A 85 LYS C . 30200 1 372 . 1 1 85 85 LYS CA C 13 59.200 0.2 . . . . . A 85 LYS CA . 30200 1 373 . 1 1 85 85 LYS CB C 13 30.867 0.2 . . . . . A 85 LYS CB . 30200 1 374 . 1 1 85 85 LYS N N 15 121.485 0.2 . . . . . A 85 LYS N . 30200 1 375 . 1 1 86 86 GLU H H 1 8.059 0.02 . . . . . A 86 GLU H . 30200 1 376 . 1 1 86 86 GLU C C 13 177.610 0.2 . . . . . A 86 GLU C . 30200 1 377 . 1 1 86 86 GLU CA C 13 57.707 0.2 . . . . . A 86 GLU CA . 30200 1 378 . 1 1 86 86 GLU CB C 13 28.730 0.2 . . . . . A 86 GLU CB . 30200 1 379 . 1 1 86 86 GLU N N 15 118.487 0.2 . . . . . A 86 GLU N . 30200 1 380 . 1 1 87 87 PHE H H 1 7.858 0.02 . . . . . A 87 PHE H . 30200 1 381 . 1 1 87 87 PHE C C 13 176.356 0.2 . . . . . A 87 PHE C . 30200 1 382 . 1 1 87 87 PHE CA C 13 59.050 0.2 . . . . . A 87 PHE CA . 30200 1 383 . 1 1 87 87 PHE CB C 13 38.675 0.2 . . . . . A 87 PHE CB . 30200 1 384 . 1 1 87 87 PHE N N 15 118.958 0.2 . . . . . A 87 PHE N . 30200 1 385 . 1 1 88 88 CYS H H 1 7.801 0.02 . . . . . A 88 CYS H . 30200 1 386 . 1 1 88 88 CYS C C 13 174.657 0.2 . . . . . A 88 CYS C . 30200 1 387 . 1 1 88 88 CYS CA C 13 60.611 0.2 . . . . . A 88 CYS CA . 30200 1 388 . 1 1 88 88 CYS CB C 13 27.445 0.2 . . . . . A 88 CYS CB . 30200 1 389 . 1 1 88 88 CYS N N 15 116.944 0.2 . . . . . A 88 CYS N . 30200 1 390 . 1 1 89 89 TYR H H 1 7.931 0.02 . . . . . A 89 TYR H . 30200 1 391 . 1 1 89 89 TYR C C 13 175.947 0.2 . . . . . A 89 TYR C . 30200 1 392 . 1 1 89 89 TYR CA C 13 58.327 0.2 . . . . . A 89 TYR CA . 30200 1 393 . 1 1 89 89 TYR CB C 13 37.922 0.2 . . . . . A 89 TYR CB . 30200 1 394 . 1 1 89 89 TYR N N 15 119.354 0.2 . . . . . A 89 TYR N . 30200 1 395 . 1 1 90 90 LYS H H 1 7.949 0.02 . . . . . A 90 LYS H . 30200 1 396 . 1 1 90 90 LYS C C 13 176.986 0.2 . . . . . A 90 LYS C . 30200 1 397 . 1 1 90 90 LYS CA C 13 56.532 0.2 . . . . . A 90 LYS CA . 30200 1 398 . 1 1 90 90 LYS CB C 13 32.068 0.2 . . . . . A 90 LYS CB . 30200 1 399 . 1 1 90 90 LYS N N 15 121.596 0.2 . . . . . A 90 LYS N . 30200 1 400 . 1 1 91 91 THR H H 1 7.995 0.02 . . . . . A 91 THR H . 30200 1 401 . 1 1 91 91 THR C C 13 174.745 0.2 . . . . . A 91 THR C . 30200 1 402 . 1 1 91 91 THR CA C 13 62.037 0.2 . . . . . A 91 THR CA . 30200 1 403 . 1 1 91 91 THR CB C 13 68.960 0.2 . . . . . A 91 THR CB . 30200 1 404 . 1 1 91 91 THR N N 15 115.681 0.2 . . . . . A 91 THR N . 30200 1 405 . 1 1 92 92 SER H H 1 8.097 0.02 . . . . . A 92 SER H . 30200 1 406 . 1 1 92 92 SER C C 13 174.370 0.2 . . . . . A 92 SER C . 30200 1 407 . 1 1 92 92 SER CA C 13 58.112 0.2 . . . . . A 92 SER CA . 30200 1 408 . 1 1 92 92 SER CB C 13 63.214 0.2 . . . . . A 92 SER CB . 30200 1 409 . 1 1 92 92 SER N N 15 118.076 0.2 . . . . . A 92 SER N . 30200 1 410 . 1 1 93 93 ALA H H 1 8.150 0.02 . . . . . A 93 ALA H . 30200 1 411 . 1 1 93 93 ALA C C 13 177.527 0.2 . . . . . A 93 ALA C . 30200 1 412 . 1 1 93 93 ALA CA C 13 52.373 0.2 . . . . . A 93 ALA CA . 30200 1 413 . 1 1 93 93 ALA CB C 13 18.193 0.2 . . . . . A 93 ALA CB . 30200 1 414 . 1 1 93 93 ALA N N 15 125.414 0.2 . . . . . A 93 ALA N . 30200 1 415 . 1 1 94 94 HIS H H 1 8.002 0.02 . . . . . A 94 HIS H . 30200 1 416 . 1 1 94 94 HIS C C 13 175.633 0.2 . . . . . A 94 HIS C . 30200 1 417 . 1 1 94 94 HIS CA C 13 55.717 0.2 . . . . . A 94 HIS CA . 30200 1 418 . 1 1 94 94 HIS CB C 13 29.844 0.2 . . . . . A 94 HIS CB . 30200 1 419 . 1 1 94 94 HIS N N 15 117.537 0.2 . . . . . A 94 HIS N . 30200 1 420 . 1 1 95 95 GLY H H 1 8.137 0.02 . . . . . A 95 GLY H . 30200 1 421 . 1 1 95 95 GLY C C 13 173.518 0.2 . . . . . A 95 GLY C . 30200 1 422 . 1 1 95 95 GLY CA C 13 44.723 0.2 . . . . . A 95 GLY CA . 30200 1 423 . 1 1 95 95 GLY N N 15 109.763 0.2 . . . . . A 95 GLY N . 30200 1 424 . 1 1 96 96 ILE H H 1 7.995 0.02 . . . . . A 96 ILE H . 30200 1 425 . 1 1 96 96 ILE CA C 13 58.184 0.2 . . . . . A 96 ILE CA . 30200 1 426 . 1 1 96 96 ILE CB C 13 37.571 0.2 . . . . . A 96 ILE CB . 30200 1 427 . 1 1 96 96 ILE N N 15 122.016 0.2 . . . . . A 96 ILE N . 30200 1 428 . 1 1 97 97 PRO C C 13 176.415 0.2 . . . . . A 97 PRO C . 30200 1 429 . 1 1 97 97 PRO CA C 13 62.794 0.2 . . . . . A 97 PRO CA . 30200 1 430 . 1 1 97 97 PRO CB C 13 31.227 0.2 . . . . . A 97 PRO CB . 30200 1 431 . 1 1 98 98 MET H H 1 8.321 0.02 . . . . . A 98 MET H . 30200 1 432 . 1 1 98 98 MET C C 13 176.152 0.2 . . . . . A 98 MET C . 30200 1 433 . 1 1 98 98 MET CA C 13 55.413 0.2 . . . . . A 98 MET CA . 30200 1 434 . 1 1 98 98 MET CB C 13 32.137 0.2 . . . . . A 98 MET CB . 30200 1 435 . 1 1 98 98 MET N N 15 120.123 0.2 . . . . . A 98 MET N . 30200 1 436 . 1 1 99 99 ILE H H 1 8.011 0.02 . . . . . A 99 ILE H . 30200 1 437 . 1 1 99 99 ILE C C 13 176.292 0.2 . . . . . A 99 ILE C . 30200 1 438 . 1 1 99 99 ILE CA C 13 60.761 0.2 . . . . . A 99 ILE CA . 30200 1 439 . 1 1 99 99 ILE CB C 13 37.827 0.2 . . . . . A 99 ILE CB . 30200 1 440 . 1 1 99 99 ILE N N 15 121.266 0.2 . . . . . A 99 ILE N . 30200 1 441 . 1 1 100 100 GLY H H 1 8.280 0.02 . . . . . A 100 GLY H . 30200 1 442 . 1 1 100 100 GLY C C 13 173.608 0.2 . . . . . A 100 GLY C . 30200 1 443 . 1 1 100 100 GLY CA C 13 44.540 0.2 . . . . . A 100 GLY CA . 30200 1 444 . 1 1 100 100 GLY N N 15 112.620 0.2 . . . . . A 100 GLY N . 30200 1 445 . 1 1 101 101 GLU H H 1 8.102 0.02 . . . . . A 101 GLU H . 30200 1 446 . 1 1 101 101 GLU C C 13 175.963 0.2 . . . . . A 101 GLU C . 30200 1 447 . 1 1 101 101 GLU CA C 13 55.558 0.2 . . . . . A 101 GLU CA . 30200 1 448 . 1 1 101 101 GLU CB C 13 29.891 0.2 . . . . . A 101 GLU CB . 30200 1 449 . 1 1 101 101 GLU N N 15 120.708 0.2 . . . . . A 101 GLU N . 30200 1 450 . 1 1 102 102 ALA H H 1 8.338 0.02 . . . . . A 102 ALA H . 30200 1 451 . 1 1 102 102 ALA CA C 13 50.071 0.2 . . . . . A 102 ALA CA . 30200 1 452 . 1 1 102 102 ALA CB C 13 17.312 0.2 . . . . . A 102 ALA CB . 30200 1 453 . 1 1 102 102 ALA N N 15 127.173 0.2 . . . . . A 102 ALA N . 30200 1 454 . 1 1 103 103 PRO C C 13 176.903 0.2 . . . . . A 103 PRO C . 30200 1 455 . 1 1 103 103 PRO CA C 13 62.468 0.2 . . . . . A 103 PRO CA . 30200 1 456 . 1 1 103 103 PRO CB C 13 31.094 0.2 . . . . . A 103 PRO CB . 30200 1 457 . 1 1 104 104 LEU H H 1 8.240 0.02 . . . . . A 104 LEU H . 30200 1 458 . 1 1 104 104 LEU C C 13 177.414 0.2 . . . . . A 104 LEU C . 30200 1 459 . 1 1 104 104 LEU CA C 13 54.731 0.2 . . . . . A 104 LEU CA . 30200 1 460 . 1 1 104 104 LEU CB C 13 41.313 0.2 . . . . . A 104 LEU CB . 30200 1 461 . 1 1 104 104 LEU N N 15 122.631 0.2 . . . . . A 104 LEU N . 30200 1 462 . 1 1 105 105 GLU H H 1 8.224 0.02 . . . . . A 105 GLU H . 30200 1 463 . 1 1 105 105 GLU C C 13 176.070 0.2 . . . . . A 105 GLU C . 30200 1 464 . 1 1 105 105 GLU CA C 13 55.846 0.2 . . . . . A 105 GLU CA . 30200 1 465 . 1 1 105 105 GLU CB C 13 29.575 0.2 . . . . . A 105 GLU CB . 30200 1 466 . 1 1 105 105 GLU N N 15 121.849 0.2 . . . . . A 105 GLU N . 30200 1 467 . 1 1 106 106 HIS H H 1 8.228 0.02 . . . . . A 106 HIS H . 30200 1 468 . 1 1 106 106 HIS CA C 13 55.662 0.2 . . . . . A 106 HIS CA . 30200 1 469 . 1 1 106 106 HIS N N 15 120.735 0.2 . . . . . A 106 HIS N . 30200 1 stop_ save_